This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nobile, S
Right arrow Articles by Deshusses, J
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nobile, S
Right arrow Articles by Deshusses, J

 Previous Article  |  Next Article 

J Bacteriol. 1988 November; 170(11): 5236-5240

research-article

Purification and properties of the gamma-butyrobetaine-binding protein from an Agrobacterium sp.

S Nobile, D Baccino, T Takagi and J Deshusses

Department of Biochemistry, University of Geneva, Switzerland.

ABSTRACT

A binding protein for gamma-butyrobetaine was purified from osmotic shock fluid of an Agrobacterium sp. It was a monomeric protein with an apparent molecular weight of 52,000 or 53,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively. The isoelectric point was 4.3, as determined by isoelectric focusing. Amino acid analysis of the protein showed that Asx and Glx were predominant components and that the protein contained no cysteine. The dissociation constant of this protein for gamma-butyrobetaine was found to be 0.7 microM by equilibrium dialysis. Attempts to sequence the amino-terminal end with the Edman method failed, suggesting that this region of the protein is blocked.

J Bacteriol. 1988 November; 170(11): 5236-5240






Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»